Abstract
There are two distinct experimental and theoretical problems of protein folding: the thermodynamic issue of characterizing the folded state, and the kinetic question of the path between the unfolded and native states1. Here we consider the second question and present a diffusion–collision–adhesion model for the folding of the α-helical protein myoglobin. In particular, we consider the fast refolding species of the unfolded state and ignore the slow transition between unfolded states that has been attributed to proline isomerization2.
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Cohen, F., Sternberg, M., Phillips, D. et al. A diffusion–collision–adhesion model for the kinetics of myoglobin refolding. Nature 286, 632–634 (1980). https://doi.org/10.1038/286632a0
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DOI: https://doi.org/10.1038/286632a0
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